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Transmembrane and ubiquitin-like domain-containing protein 1 (Dendritic cell-derived ubiquitin-like protein) (DULP) (Hepatocyte odd protein shuttling protein) (Ubiquitin-like protein SB144) [Cleaved into: iHOPS]

 TMUB1_HUMAN             Reviewed;         246 AA.
Q9BVT8; D3DX06; Q53AQ2;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 132.
RecName: Full=Transmembrane and ubiquitin-like domain-containing protein 1;
AltName: Full=Dendritic cell-derived ubiquitin-like protein;
Short=DULP;
AltName: Full=Hepatocyte odd protein shuttling protein;
AltName: Full=Ubiquitin-like protein SB144;
Contains:
RecName: Full=iHOPS;
Name=TMUB1; Synonyms=C7orf21, DULP, HOPS;
ORFNames=SB144, UNQ763/PRO1555;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16014383; DOI=10.1242/jcs.02452;
Della Fazia M.A., Castelli M., Bartoli D., Pieroni S., Pettirossi V.,
Piobbico D., Viola-Magni M., Servillo G.;
"HOPS: a novel cAMP-dependent shuttling protein involved in protein
synthesis regulation.";
J. Cell Sci. 118:3185-3194(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Dendritic cell;
PubMed=19254477; DOI=10.1038/cmi.2009.4;
Liu G.Y., Liu S.X., Li P., Tang L., Han Y.M., An H.Z., Li J.Y.,
Dai X.K., Li N., Cao X.T., Yu Y.Z.;
"Cloning and characterization of DULP, a novel ubiquitin-like molecule
from human dendritic cells.";
Cell. Mol. Immunol. 6:27-33(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; THR-92 AND SER-98,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-98, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
FUNCTION, AND INTERACTION WITH ERLIN2 AND AMFR.
PubMed=21343306; DOI=10.1074/jbc.M110.211326;
Jo Y., Sguigna P.V., DeBose-Boyd R.A.;
"Membrane-associated ubiquitin ligase complex containing gp78 mediates
sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme
A reductase.";
J. Biol. Chem. 286:15022-15031(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-73 AND SER-127,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
TISSUE SPECIFICITY.
PubMed=24240191; DOI=10.4161/cc.27054;
Castelli M., Piobbico D., Bartoli D., Pieroni S., Brunacci C.,
Bellet M.M., Chiacchiaretta M., Della Fazia M.A., Servillo G.;
"Different functions of HOPS isoforms in the cell: HOPS shuttling
isoform is determined by RIP cleavage system.";
Cell Cycle 13:293-302(2014).
-!- FUNCTION: Involved in sterol-regulated ubiquitination and
degradation of HMG-CoA reductase HMGCR (PubMed:21343306). Involved
in positive regulation of AMPA-selective glutamate receptor GRIA2
recycling to the cell surface (By similarity). Acts as negative
regulator of hepatocyte growth during regeneration (By
similarity). {ECO:0000250|UniProtKB:Q53AQ4,
ECO:0000250|UniProtKB:Q9JMG3, ECO:0000269|PubMed:21343306}.
-!- FUNCTION: iHOPS: May contribute to the regulation of translation
during cell-cycle progression. May contribute to the regulation of
cell proliferation (By similarity). May be involved in centrosome
assembly. Modulates stabilization and nucleolar localization of
tumor suppressor CDKN2A and enhances association between CDKN2A
and NPM1 (By similarity). {ECO:0000250|UniProtKB:Q9JMG3}.
-!- SUBUNIT: Interacts with EEF1A1, GRIA2, GRIP1, CAMLG, TUBG1 (By
similarity). Interacts with NPM1 and CDKN2A; TMUB1 can enhance
interaction between NPM1 and CDKN2A and is proposed to bridge the
proteins; proposed to be mediated by iHOPS (By similarity).
Interacts with ERLIN2 and AMFR; TMUB1 promotes the interaction of
ERLIN2 with AMFR (PubMed:21343306). {ECO:0000250|UniProtKB:Q53AQ4,
ECO:0000250|UniProtKB:Q9JMG3, ECO:0000269|PubMed:21343306}.
-!- INTERACTION:
O94905:ERLIN2; NbExp=5; IntAct=EBI-11425701, EBI-4400770;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9JMG3};
Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JMG3}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:Q9JMG3}. Recycling endosome
{ECO:0000250|UniProtKB:Q53AQ4}. Cytoplasm
{ECO:0000250|UniProtKB:Q9JMG3}. Nucleus
{ECO:0000250|UniProtKB:Q9JMG3}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q9JMG3}.
-!- SUBCELLULAR LOCATION: iHOPS: Cytoplasm
{ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9JMG3}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q9JMG3}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q9JMG3}. Nucleus
{ECO:0000250|UniProtKB:Q9JMG3}. Note=iHOPS is proposed to be the
shuttling form across different cellular compartments. XPO1-
dependent exported from the nucleus in dividing cells.
Predominantly nuclear during growth arrest.
{ECO:0000250|UniProtKB:Q9JMG3}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
mammary and thyroid glands, bone marrow and spleen; limited
expression in cardiac, pancreatic and ovarian tissues.
{ECO:0000269|PubMed:24240191}.
-!- PTM: iHOPS: Processed by regulated intramembrane proteolysis
(RIP)in the N-terminus to release iHOPS from membranes (By
similarity). {ECO:0000250|UniProtKB:Q9JMG3}.
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EMBL; AY603380; AAU00156.1; -; mRNA.
EMBL; AY037155; AAK67645.1; -; mRNA.
EMBL; AY358481; AAQ88845.1; -; mRNA.
EMBL; AK314035; BAG36745.1; -; mRNA.
EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471173; EAW54030.1; -; Genomic_DNA.
EMBL; CH471173; EAW54032.1; -; Genomic_DNA.
EMBL; BC000936; AAH00936.1; -; mRNA.
EMBL; BC033182; AAH33182.1; -; mRNA.
CCDS; CCDS5920.1; -.
RefSeq; NP_001129516.1; NM_001136044.1.
RefSeq; NP_113622.1; NM_031434.3.
UniGene; Hs.726215; -.
ProteinModelPortal; Q9BVT8; -.
SMR; Q9BVT8; -.
BioGrid; 123686; 35.
IntAct; Q9BVT8; 5.
STRING; 9606.ENSP00000297533; -.
TCDB; 8.A.62.1.1; the transmembrane and ubiquitin-like domain-containing protein 1 (tmub1) family.
iPTMnet; Q9BVT8; -.
PhosphoSitePlus; Q9BVT8; -.
BioMuta; TMUB1; -.
DMDM; 34922062; -.
EPD; Q9BVT8; -.
MaxQB; Q9BVT8; -.
PaxDb; Q9BVT8; -.
PeptideAtlas; Q9BVT8; -.
PRIDE; Q9BVT8; -.
TopDownProteomics; Q9BVT8; -.
Ensembl; ENST00000297533; ENSP00000297533; ENSG00000164897.
Ensembl; ENST00000392818; ENSP00000376565; ENSG00000164897.
Ensembl; ENST00000462940; ENSP00000417519; ENSG00000164897.
Ensembl; ENST00000476627; ENSP00000419214; ENSG00000164897.
Ensembl; ENST00000482202; ENSP00000418709; ENSG00000164897.
GeneID; 83590; -.
KEGG; hsa:83590; -.
UCSC; uc003wjb.4; human.
CTD; 83590; -.
DisGeNET; 83590; -.
EuPathDB; HostDB:ENSG00000164897.12; -.
GeneCards; TMUB1; -.
HGNC; HGNC:21709; TMUB1.
HPA; HPA029429; -.
MIM; 614792; gene.
neXtProt; NX_Q9BVT8; -.
OpenTargets; ENSG00000164897; -.
PharmGKB; PA134863959; -.
eggNOG; ENOG410IG1T; Eukaryota.
eggNOG; ENOG4111WH7; LUCA.
GeneTree; ENSGT00390000014069; -.
HOGENOM; HOG000232067; -.
HOVERGEN; HBG050920; -.
InParanoid; Q9BVT8; -.
OMA; CVLHCHI; -.
OrthoDB; EOG091G0NYR; -.
PhylomeDB; Q9BVT8; -.
TreeFam; TF329265; -.
ChiTaRS; TMUB1; human.
GenomeRNAi; 83590; -.
PMAP-CutDB; Q9BVT8; -.
PRO; PR:Q9BVT8; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000164897; -.
CleanEx; HS_TMUB1; -.
ExpressionAtlas; Q9BVT8; baseline and differential.
Genevisible; Q9BVT8; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF00240; ubiquitin; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Endosome; Membrane; Nucleus; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Synapse;
Transmembrane; Transmembrane helix.
CHAIN 1 246 Transmembrane and ubiquitin-like domain-
containing protein 1.
/FTId=PRO_0000114922.
CHAIN ? 246 iHOPS.
/FTId=PRO_0000435488.
TRANSMEM 11 31 Helical. {ECO:0000255}.
TRANSMEM 195 215 Helical. {ECO:0000255}.
TRANSMEM 221 241 Helical. {ECO:0000255}.
DOMAIN 103 176 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
REGION 2 30 Required to release iHOPS from membranes.
{ECO:0000250|UniProtKB:Q9JMG3}.
MOD_RES 71 71 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 92 92 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
SEQUENCE 246 AA; 26261 MW; E08E25A6B37665B3 CRC64;
MTLIEGVGDE VTVLFSVLAC LLVLALAWVS THTAEGGDPL PQPSGTPTPS QPSAAMAATD
SMRGEAPGAE TPSLRHRGQA AQPEPSTGFT ATPPAPDSPQ EPLVLRLKFL NDSEQVARAW
PHDTIGSLKR TQFPGREQQV RLIYQGQLLG DDTQTLGSLH LPPNCVLHCH VSTRVGPPNP
PCPPGSEPGP SGLEIGSLLL PLLLLLLLLL WYCQIQYRPF FPLTATLGLA GFTLLLSLLA
FAMYRP


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EIAAB44725 Deubiquitinating enzyme 17-like protein 1,Homo sapiens,Human,Putative ubiquitin carboxyl-terminal hydrolase 17-like protein 1,Ubiquitin thiolesterase 17-like protein 1,Ubiquitin-specific-processing pr
EIAAB45123 Cbl-interacting protein 4,CLIP4,Homo sapiens,Human,STS2,STS-2,Suppressor of T-cell receptor signaling 2,T-cell ubiquitin ligand,TULA,UBASH3A,Ubiquitin-associated and SH3 domain-containing protein A
18-003-44311 Ubiquitin-conjugating enzyme E2-25 kDa - EC 6.3.2.19; Ubiquitin-protein ligase; Ubiquitin carrier protein; E2(25K); Huntingtin-interacting protein 2; HIP-2 Polyclonal 0.1 mg Protein A
EIAAB44754 Homo sapiens,Human,Putative ubiquitin-conjugating enzyme E2 D2-like protein,UBE2D2L,UBE2DNL,Ubiquitin carrier protein D2-like,Ubiquitin-conjugating enzyme E2D N-terminal-like,Ubiquitin-protein ligase
18-661-15203 E3 ubiquitin ligase TRIAD3 - EC 6.3.2.-; Ubiquitin-conjugating enzyme 7-interacting protein 1; Zinc finger protein inhibiting NF-kappa-B; Triad domain-containing protein 3 Polyclonal 0.1 mg
EIAAB45297 E3 ubiquitin-protein ligase UHRF1,Mouse,Mus musculus,Np95,Nuclear protein 95,Nuclear zinc finger protein Np95,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing P
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB40559 GAP-modifying protein 1,GMP1,Homo sapiens,Human,OK_SW-cl.43,Sentrin,Small ubiquitin-related modifier 1,SMT3 homolog 3,Smt3C,SMT3C,SMT3H3,SUMO1,SUMO-1,Ubiquitin-homology domain protein PIC1,Ubiquitin-l
EIAAB40561 Mouse,Mus musculus,Small ubiquitin-related modifier 1,SMT3 homolog 3,Smt3C,Smt3c,Smt3h3,Sumo1,SUMO-1,Ubiquitin-homology domain protein PIC1,Ubiquitin-like protein SMT3C,Ubl1


 

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